Teaster Baird

Biochemistry
My research interests revolve around understanding the relationship
between the structures of certain proteins, namely metallo-enzymes and
proteases, and their functions. Our understanding of how the three
dimensional structure of a protein dictates its function is limited.
However, by examining known protein structures and making both
semi-random and logical changes in the structure of a protein, we can
rationalize how certain structural features give rise to certain
aspects of its function. In some cases, this understanding can allow
one to predictably introduce new functionalities into existing protein
scaffolds. Experiments in my laboratory will be focused on designing
and introducing metal binding sites into serine proteases to
investigate their mechanisms of activation, altering serine protease
structure to introduce new catalytic machinery, and examining catalytic
and structural zinc binding sites in zinc metallo-proteins to dissect
the factors that determine how the metal is used. Techniques used to
design, produce and characterize the engineered proteins will include
site-directed and random mutagenesis, computer modeling, the
incorporation of non-natural amino acids and UV-Vis and fluorescence
spectroscopy.